| Abstrakt: |
We have utilized anin vitroassay that measures the binding of an L-selectin-human Fc chimera (LS-Fc) to [35S]sulfate labelled peripheral addressin (PNAd), a 120 kDa glycoprotein ligand for L-selectin in porcine lymph nodes, to evaluate inhibitory properties of a small group of sulfated derivatives of β-cyclodextrin (β-CD), sLexandmyo-inositol to their non-sulfated counterparts were studied. We found that hepta-sulfated β-CD (IC50= 0.2 mM) strongly inhibited the binding of L-selectin to PNAd. In contrast, the monosulfated β-CD was a poor inhibitor, displaying <10% inhibition at 0.5 mM and β-CD was not active as an inhibitor. Similarly, inositol hexakissulfate, a compound containing six sulfate groups on the inositol ring displayed an inhibition of about 61% at 0.5 mM concentration, whereas the non-sulfatedmyo-inositol was not inhibitory. These findings provide evidence that clustering of sulfate groups enhances affinity of molecules for binding to L-selectin. |
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